Abstract:
:Upon dimerization by oxidation, Hsp33 functions as a molecular chaperone in prokaryotes. Previously published structures of both the inactive and active species are of doubtful relevance to the solution conformations since the inactive (reduced) crystal structure was dimeric, while the active (oxidized) species was crystallized with a truncation of its regulation domain. The interdomain contact site of the inactive monomer, identified in this work, is consistent with that previously observed in the reduced dimer crystal. In contrast, fluorescence quenching of the active dimer contradicted the results expected from the domain-swapped fold observed in the truncated dimer crystal. The results of this study provide important new information concerning controversial issues in the activation process of Hsp33.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lee YS,Ryu KS,Kim SJ,Ko HS,Sim DW,Jeon YH,Kim EH,Choi WS,Won HSdoi
10.1016/j.febslet.2012.01.011subject
Has Abstractpub_date
2012-02-17 00:00:00pages
411-5issue
4eissn
0014-5793issn
1873-3468pii
S0014-5793(12)00031-2journal_volume
586pub_type
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